Kafatos:Povelones, Michael: Difference between revisions
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* [[pmid:16085697|Povelones M, Howes R, Fish M, and Nusse R. Genetic evidence that Drosophila frizzled controls planar cell polarity and Armadillo signaling by a common mechanism. Genetics 2005 Dec; 171(4) 1643-54.]] | * [[pmid:16085697|Povelones M, Howes R, Fish M, and Nusse R. Genetic evidence that Drosophila frizzled controls planar cell polarity and Armadillo signaling by a common mechanism. Genetics 2005 Dec; 171(4) 1643-54.]] | ||
* [[pmid:12415278|Povelones M and Nusse R. Wnt signalling sees spots. Nat Cell Biol 2002 Nov; 4(11) E249-50.]] | * [[pmid:12415278|Povelones M and Nusse R. Wnt signalling sees spots. Nat Cell Biol 2002 Nov; 4(11) E249-50.]] | ||
* [[pmid: 18555784|Chen WS, Antic D, Matis M, Logan CY, Povelones M, Anderson GA, Nusse R, Axelrod JD. Asymmetric homotypic interactions of the atypical cadherin flamingo mediate intercellular polarity signaling. Cell. 2008 Jun 13;133(6):1093-105.]] | |||
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Michael Povelones
Division of Cell & Molecular Biology
Imperial College |
Education
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Current Research InterestsI am a postdoctoral fellow in the Kafatos/Christophides Lab at Imperial College, London. Science is cool. |
Previous ResearchI received my doctoral degree at Stanford University in the laboratory of Roel Nusse. The focus of my research was understanding how the frizzled (fz) receptor in Drosophila functions in planar cell polarization (PCP) and Wnt-mediated cell fate specification. fz controls two different signal transduction pathways for each of these distinct developmental outcomes. How does a single receptor function in two signaling pathways? This work revealed that even though cell fate signaling requires a Wnt ligand, fz is not activated by any of the 7 Drosophila Wnt genes for its PCP function. Instead, fz has an intrinsic ability to control components of the PCP pathway and that it associates with pathway specific Wnt co-receptor for cell fate signaling. In addition, a structure-function analysis of fz suggested that, in addition to the Wnt binding site located in the extracellular cysteine-rich domain, there is a second Wnt-binding site within the transmembrane portion of the receptor.
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